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undergraduate thesis
Kolagen i utjecaj njegovih peptida na strukturu kože
Split: University of Split, Faculty of Science, 2022. urn:nbn:hr:166:986122
Župić, Sara
University of Split
Faculty of Science
Department of Chemistry

Institutional repository: Repository of Faculty of Science

Cite this document

Župić, S. (2022). Kolagen i utjecaj njegovih peptida na strukturu kože (Undergraduate thesis). Split: University of Split, Faculty of Science. Retrieved from https://urn.nsk.hr/urn:nbn:hr:166:986122

Župić, Sara. "Kolagen i utjecaj njegovih peptida na strukturu kože." Undergraduate thesis, University of Split, Faculty of Science, 2022. https://urn.nsk.hr/urn:nbn:hr:166:986122

Župić, Sara. "Kolagen i utjecaj njegovih peptida na strukturu kože." Undergraduate thesis, University of Split, Faculty of Science, 2022. https://urn.nsk.hr/urn:nbn:hr:166:986122

Župić, S. (2022). 'Kolagen i utjecaj njegovih peptida na strukturu kože', Undergraduate thesis, University of Split, Faculty of Science, accessed 27 April 2024, https://urn.nsk.hr/urn:nbn:hr:166:986122

Župić S. Kolagen i utjecaj njegovih peptida na strukturu kože [Undergraduate thesis]. Split: University of Split, Faculty of Science; 2022 [cited 2024 April 27] Available at: https://urn.nsk.hr/urn:nbn:hr:166:986122

S. Župić, "Kolagen i utjecaj njegovih peptida na strukturu kože", Undergraduate thesis, University of Split, Faculty of Science, Split, 2022. Available at: https://urn.nsk.hr/urn:nbn:hr:166:986122

Metadata
TitleKolagen i utjecaj njegovih peptida na strukturu kože
Title (english)Collagen and the influence of its peptides on skin structure
AuthorSara Župić
MentorBarbara Soldo (mentor)
Committee memberBarbara Soldo (predsjednik povjerenstva)
Committee memberRoko Vladušić (član povjerenstva)
Committee memberMatilda Šprung (član povjerenstva)
GranterUniversity of Split
Faculty of Science
(Department of Chemistry)
Split
Defense date and country2022-09-27, Croatia
Scientific / art field,
discipline and subdiscipline		NATURAL SCIENCES
Chemistry
Abstract
Kolagen je najprisutniji protein u čovjekovu tijelu. Ima strukturu trostruke zavojnice i određeni sadržaj aminokiselina. Stanicama daje čvrstoću i potporu zbog stabiliziranosti unutarmolekulskim interakcijama. Sintetiziraju ga fibroblasti. Fibroblasti sintetiziraju i druge komponente izvanstaničnog matriksa. Tijekom godina, zbog nakupljanja oštećenih i pogrešno strukturiranih proteina, koža gubi svoja svojstva te se različitim metodama pokušava taj proces usporiti. Najznačajnija je primjena peptida kolagena koji nastaju djelovanjem enzima na denaturirani kolagen koji zbog svojih svojstava potiču stvaranje kolagenih vlakana, potiču sintezu hijaluronske kiseline i diobu stanica fibroblasta.
Abstract (english)
Collagen is the most abundant protein in the human body. It has a structure of triple helix and a specific content of amino acids. It gives strength and support to cells as it is stabilized by intramolecular interactions. It is synthesized by fibroblasts. Fibroblasts also synthesize other components of the extracellular matrix. Over the years, the skin loses its properties due to the accumulation of damaged and misstructured proteins, and various methods are used to slow down this process. The most important method is the application of collagen peptides, which are produced by the action of enzymes on denatured collagen and due to their properties stimulate the formation of collagen fibers, the synthesis of hylauronic acid and the division of fibroblast cells.
Keywords
Keywords (english)
Languagecroatian
URN:NBNurn:nbn:hr:166:986122
Study programmeTitle: Biology and Chemistry
Study programme type: university
Study level: undergraduate
Academic / professional title: sveučilišni/a prvostupnik/prvostupnica (baccalaureus/baccalaurea) biologije i kemije (sveučilišni/a prvostupnik/prvostupnica (baccalaureus/baccalaurea) biologije i kemije)
Type of resourceText
File originBorn digital
Access conditionsOpen access
Terms of useLicence Attribution-NoDerivatives 4.0 International (CC BY-ND 4.0) icon
Created on2023-03-02 12:52:35